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© Perrine Bomme, Guillaume Duménil, Jean-Marc Panaud.
Coloured scanning electron micrograph (SEM) of Neisseria meningitidis on epithelial cells
Publication : The Journal of biological chemistry

Detailed structural analysis of the peptidoglycan of the human pathogen Neisseria meningitidis.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Journal of biological chemistry - 10 Jun 2003

Antignac A, Rousselle JC, Namane A, Labigne A, Taha MK, Boneca IG,

Link to Pubmed [PMID] – 12799361

J Biol Chem 2003 Aug; 278(34): 31521-8

We used reverse-phase high pressure liquid chromatography (HPLC), matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS) and post source decay analysis (MALDI-PSD) to determine the muropeptide composition of the human pathogen Neisseria meningitidis. Structural assignment was determined for 28 muropeptide species isolated after HPLC separation and purification. Fourteen of these muropeptides were O-acetylated to different degrees. We identified the entire O-acetylation spectrum of dimers and trimers both in muropeptides and 1,6-anhydromuropeptides. On average, one of three disaccharides was O-acetylated. Furthermore, the degree of cross-linking of the N. meningitidis peptidoglycan was around 39% in all the strains analyzed. MALDI-PSD analysis of several muropeptide species indicated that meningococci only synthesize D-alanyl-meso-diaminopimelate cross-bridges. No muropeptides representative of covalent linkages of lipoproteins to the peptidoglycan could be identified, unlike in Escherichia coli. Finally, comparison of the muropeptide composition of penicillin-susceptible and penicillin-intermediate clinical strains of meningococci showed a positive correlation between the minimum inhibitory concentration (MIC) of penicillin G and the amount of muropeptides carrying an intact pentapeptide chain in the peptidoglycan. This suggests that reduced susceptibility to penicillin G in N. meningitidis is associated with a decrease in d,d-carboxypeptidase activity and/or D,D-transpeptidase activity.